Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating - Wikidata - wikimedia - TriplyDB

Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

http://www.wikidata.org/entity/Q37395175

about

KCNQ potassium channels in sensory system and neural circuits Nanoscale monitoring of drug actions on cell membrane using atomic force microscopy Human EAG channels are directly modulated by PIP2 as revealed by electrophysiological and optical interference investigations Regulation of KCNQ/Kv7 family voltage-gated K+ channels by lipids.PIP₂-dependent coupling is prominent in Kv7.1 due to weakened interactions between S4-S5 and S6.Conservation analysis of residues in the S4-S5 linker and the terminal part of the S5-P-S6 pore modulus in Kv and HCN channels: flexible determinants for the electromechanical coupling.Migration of PIP2 lipids on voltage-gated potassium channel surface influences channel deactivation The Voltage Activation of Cortical KCNQ Channels Depends on Global PIP2 Levels.Osmoregulatory inositol transporter SMIT1 modulates electrical activity by adjusting PI(4,5)P2 levels PIP2 regulation of KCNQ channels: biophysical and molecular mechanisms for lipid modulation of voltage-dependent gating.Modulation of Kv7 channels and excitability in the brain.Competition of calcified calmodulin N lobe and PIP2 to an LQT mutation site in Kv7.1 channel.Phosphorylation regulates the sensitivity of voltage-gated Kv7.2 channels towards phosphatidylinositol-4,5-bisphosphate.Chansporter complexes in cell signaling.Molecular determinants of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) binding to transient receptor potential V1 (TRPV1) channels.Early-onset epileptic encephalopathy caused by a reduced sensitivity of Kv7.2 potassium channels to phosphatidylinositol 4,5-bisphosphate.Ion channel regulation by phosphoinositides analyzed with VSPs-PI(4,5)P2 affinity, phosphoinositide selectivity, and PI(4,5)P2 pool accessibility.Phosphoinositol-4,5-Bisphosphate Regulates Auditory Hair-Cell Mechanotransduction-Channel Pore Properties and Fast Adaptation.KCNQ-SMIT complex formation facilitates ion channel-solute transporter cross talk.PIP2 mediates functional coupling and pharmacology of neuronal KCNQ channels.Migration of PIP2 on KCNQ2 Surface Revealed by Molecular Dynamics Simulations.Intracellular zinc activates KCNQ channels by reducing their dependence on phosphatidylinositol 4,5-bisphosphate.

P2860

Q26774667-27A24599-9953-4F75-A08A-C57132014D72 Q26852240-F45203D6-B43B-4E10-8B57-2AC7C9CF7ACD Q28118681-6EDB8D6E-3042-4AC4-A629-7A334B7BB56D Q30394930-EC5560A4-6628-4F8D-B91A-7313ADEE4A4E Q34830254-837C35DF-7C01-4678-B513-543944122BA6 Q35422054-E89582AF-6D59-43C8-928C-2EB04B763D9D Q36164522-BE2462D5-0E07-4FF6-BE8E-E1D148AA51E0 Q36678567-30647049-B0B6-4D79-B686-9417934DA436 Q37183615-F9C1E5F3-7BBE-4927-84D6-3CEC3057035B Q38218095-AE6A1383-36DB-4572-89B5-97DAD47A46BA Q38958968-EF4DA4D4-A209-4EF8-96DC-A19E142BE376 Q39016123-61116AF3-4848-40F3-83B6-89A04F8DE4FF Q39398244-DC3609E0-7E03-41AB-B4E4-07707CF9BF25 Q39441418-3EE96D3E-AC7E-4B63-8088-D68D9BD4D2BF Q41882659-8D4BE5F1-215E-4690-A512-89D451C7D26B Q41895295-82F09C8F-29FB-47AE-A6E5-DCE664247E66 Q42422918-9A5C97E4-9839-4068-931B-4136E3956499 Q42698907-D6AC4E4D-7DC8-4967-A3A0-84651611A4E2 Q45996705-B2EDE7B1-5FCD-4BE2-84D9-ABF8D7A11301 Q46335684-29A5DF53-10DF-4B10-B9EE-3A8CF4757594 Q47617911-9C54E05F-6640-4DAD-B5F8-0B1362FF9F26 Q48112896-072121E4-E293-420F-9E2B-0C8623B0DAD0

P2860

Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

http://www.wikidata.org/entity/Q37395175

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年学术文章

@wuu

2013年学术文章

@zh-cn

2013年学术文章

@zh-hans

2013年学术文章

@zh-my

2013年学术文章

@zh-sg

2013年學術文章

@yue

2013年學術文章

@zh

2013年學術文章

@zh-hant

name

Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

@en

Dynamic PIP2 interactions with ...... ibute to KCNQ2 channel gating.

@nl

type

label

Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

@en

Dynamic PIP2 interactions with ...... ibute to KCNQ2 channel gating.

@nl

prefLabel

Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

@en

Dynamic PIP2 interactions with ...... ibute to KCNQ2 channel gating.

@nl

P1433

Q37395175-5C9FC0D1-67F8-411B-A593-515DA032C8E2

P1476

Q37395175-F39BA8D8-3236-4C12-AE65-5DB9D7482244

P2093

Q37395175-623F2689-6E2C-43BB-8FF0-F9B5FC4B6A43

Q37395175-71DFA5EF-9007-4C09-96AC-08BB6E7AE248

Q37395175-7D879DBF-7CB9-4532-9C80-143AACBBF903

Q37395175-A606EB26-7E6C-484C-A7B4-CB92125776F5

Q37395175-BF531A96-14FC-427E-A8DE-47420EA35B7C

Q37395175-F2424FCB-955D-4FD9-A97B-B3ED67375384

P2860

Q37395175-062533C6-0756-4D6D-836F-36758E7F2DA1

Q37395175-08804861-6794-4434-B2A4-532973B2AB2C

Q37395175-0C788E6C-450D-4D65-BE78-4F559C1657D1

Q37395175-0E06A3EC-2067-48C2-9702-2F702B91B766

Q37395175-0FA118B1-5F7F-45D6-AA96-DFD04C1899CD

Q37395175-1059755D-3B4D-4881-9C1C-019607261DF8

Q37395175-135F61DD-C93F-4F67-BD79-5F4B77544D72

Q37395175-1F2FD076-18F4-4A7E-8FF1-4B6F71C04AA4

Q37395175-23FDD7C6-9CFC-46CD-AF58-B4B4EE71258A

Q37395175-263180F8-4CE0-4500-BC3F-E235976DC4B1

P304

Q37395175-987240B5-0403-490E-B6B2-A591342D6BB0

P31

Q37395175-E868AE87-8232-4C4F-B621-C7A7EF6FEC29

P356

Q37395175-8DC49A60-70C3-4B13-A96A-0F737A8FE8E4

P407

Q37395175-81B5B328-045C-4B1D-B9EE-FCD4E0666835

P433

Q37395175-4D83EAA3-48DD-44B9-BECD-B3B373ED3AF7

P478

Q37395175-F3E5F146-D02C-4576-921B-1FB4288FFE2E

P50

Q37395175-462F7473-2C48-4E47-9ABE-5E1597F88789

P577

Q37395175-C2616ED0-77B9-46EB-A5A3-C21E8FC3BAE7

P698

Q37395175-FF23FDF1-B14E-4E3B-9CDA-2F11A720E54F

P932

Q37395175-62A9E3C4-5140-4140-94D9-E5C7D5E31932

P356

PNAS.1312483110

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating

@en

P2093

Hualiang Jiang

http://www.w3.org/2001/XMLSchema#string

Min Li

http://www.w3.org/2001/XMLSchema#string

Pingzheng Zhou

http://www.w3.org/2001/XMLSchema#string

Qiansen Zhang

http://www.w3.org/2001/XMLSchema#string

Zhaobing Gao

http://www.w3.org/2001/XMLSchema#string

Zhuxi Chen

http://www.w3.org/2001/XMLSchema#string

P2860

Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2

Mechanism of activation gating in the full-length KcsA K+ channel

Crystal structure of full-length KcsA in its closed conformation

Crystal Structure of the Mammalian GIRK2 K+ Channel and Gating Regulation by G Proteins, PIP2, and Sodium

X-ray structure of the mammalian GIRK2–βγ G-protein complex

All-atom empirical potential for molecular modeling and dynamics studies of proteins

GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

Crystal structure of a mammalian voltage-dependent Shaker family K+ channel

Canonical sampling through velocity rescaling

Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types.

P304

20093-20098

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.1312483110

http://www.w3.org/2001/XMLSchema#string

P407

P433

50

http://www.w3.org/2001/XMLSchema#string

P478

110

http://www.w3.org/2001/XMLSchema#string

P50

P577

2013-11-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

24277843

http://www.w3.org/2001/XMLSchema#string

P932

3864334

http://www.w3.org/2001/XMLSchema#string